INT196910

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Context Info
Confidence 0.45
First Reported 2006
Last Reported 2006
Negated 1
Speculated 0
Reported most in Body
Documents 1
Total Number 2
Disease Relevance 0.81
Pain Relevance 0

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

nucleus (Rb1) enzyme binding (Rb1) cell cycle (Rb1)
DNA binding (Rb1) cell division (Rb1) transcription factor binding (Rb1)
Rb1 (Mus musculus)
Pain Link Frequency Relevance Heat
headache 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Pituitary Cancer 54 94.36 High High
Cancer 6 80.00 Quite High
Targeted Disruption 22 79.20 Quite High
Retinoblastoma 4 60.84 Quite High
Repression 4 38.76 Quite Low
Adenoma 8 32.80 Quite Low
Prolactinoma 6 5.00 Very Low Very Low Very Low
Syndrome 2 5.00 Very Low Very Low Very Low
Headache 2 5.00 Very Low Very Low Very Low
Hypopituitarism 2 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Interestingly, this positive role of HMGA2 on cell proliferation is due to the interaction with pRB, opening a new class of cell cycle related proteins: "the suppressors of the cell cycle inhibitors".
Positive_regulation (due) of pRB Binding (interaction) of
1) Confidence 0.45 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.35 Pain Relevance 0
However, what appears to be really novel, is the mechanism that leads to E2F1 activation by HMGA2: the E2F1 protein is not displaced from the pRB complex, but an increased acetylation that is dependent on the removal of HDAC1 from pRB takes place.
Neg (not) Positive_regulation (displaced) of pRB Binding (complex) of
2) Confidence 0.45 Published 2006 Journal Cell Div Section Body Doc Link PMC1563461 Disease Relevance 0.46 Pain Relevance 0

General Comments

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